title: Biochemical characterization of tyrosinase inhibitors using tyrosinase binding affinity chromatography.
abstract: Purification of tyrosinase inhibitors of hamster melanomas was carried out using tyrosinase binding affinity column chromatography. This method enables the isolation of tyrosinase inhibitors with a 124-fold purification index as compared to that of crude preparation after dialysation. The purified inhibitors consist of a mixture of 5000-6000 and a 310 molecular weight fraction. They also show characteristics of polypeptides which contain glycine, glutamic acid, serine, proline and alanine as main amino acids.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004156:Catechol Oxidase / Q000037:antagonists & inhibitors*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D006224:Cricetinae; D008545:Melanoma / Q000032:analysis; D008970:Molecular Weight; D014442:Monophenol Monooxygenase / Q000037:antagonists & inhibitors*; D009374:Neoplasms, Experimental / Q000032:analysis; D010455:Peptides / Q000302:isolation & purification
chemical_list: D000596:Amino Acids; D010455:Peptides; D004156:Catechol Oxidase; D014442:Monophenol Monooxygenase